Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 진언선 | - |
dc.date.accessioned | 2022-11-02T04:47:28Z | - |
dc.date.available | 2022-11-02T04:47:28Z | - |
dc.date.issued | 2021-02 | - |
dc.identifier.citation | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, v. 175, page. 341-350 | en_US |
dc.identifier.issn | 0141-8130; 1879-0003 | en_US |
dc.identifier.uri | https://www.sciencedirect.com/science/article/pii/S0141813021003032?via%3Dihub | en_US |
dc.identifier.uri | https://repository.hanyang.ac.kr/handle/20.500.11754/176204 | - |
dc.description.abstract | Enzyme immobilization using inorganic materials has been shown to preserve enzyme activity improving and improve their practical applications in biocatalytic process designs. Proper immobilization methods have been used to obtain high recycling and storage stability. In this study, we compared the activity and stability of in situ or crosslink-immobilized enzymes in a CaCO3 biomineral carrier. More than 30% of the initial enzyme activity was preserved for both the systems after 180 days upon 15 activity measurements at room temperature, confirming the improved stability of these enzyme systems (100 mM phosphate buffer, pH 8.0); however, differences in enzyme loading, activity, and characteristics were observed for each of these methods. Each system exhibited efficacy of 80% and 20%, respectively. Based on the same amount of immobilized enzyme (0.2 mg), the specific activities of hydrolysis of p-nitrophenyl butyrate substrate at room temperature of in situ immobilized carboxyl esterase (CE) and crosslinked CE were 11.37 and 7.63 mM min-1 mg-1, respectively (100 mM phosphate buffer, pH 8.0). Moreover, based on the kinetic behavior, in situ immobilized CE exhibited improved catalytic efficiency (Vmax Km-1) of the enzyme, exhibiting 4-fold higher activity and efficiency values than those of the CE immobilized in CaCO3. This is the first study to describe the stabilization of enzymes in CaCO3 and compare the enzyme kinetics and efficiencies between in situ immobilization and crosslinking in CaCO3 carriers. | en_US |
dc.description.sponsorship | This work was supported by the Dong-A University research fund. | en_US |
dc.language | en | en_US |
dc.publisher | ELSEVIER | en_US |
dc.subject | Enzyme stabilization; Enzyme immobilization; in situ immobilization calcium carbonate; Inorganic material | en_US |
dc.title | Evaluating enzyme stabilizations in calcium carbonate: Comparing in situ and crosslinking mediated immobilization | en_US |
dc.type | Article | en_US |
dc.relation.no | 8130 | - |
dc.relation.volume | 141 | - |
dc.identifier.doi | 10.1016/j.ijbiomac.2021.02.028 | en_US |
dc.relation.page | 1-10 | - |
dc.relation.journal | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | - |
dc.contributor.googleauthor | Lee, Chan Hee | - |
dc.contributor.googleauthor | Lee, Hye Sun | - |
dc.contributor.googleauthor | Lee, Jae Won | - |
dc.contributor.googleauthor | Kim, Jangyong | - |
dc.contributor.googleauthor | Lee, Jin Hyung | - |
dc.contributor.googleauthor | Jin, Eon Seon | - |
dc.contributor.googleauthor | Hwang, Ee Taek | - |
dc.relation.code | 2021004252 | - |
dc.sector.campus | S | - |
dc.sector.daehak | COLLEGE OF NATURAL SCIENCES[S] | - |
dc.sector.department | DEPARTMENT OF LIFE SCIENCE | - |
dc.identifier.pid | esjin | - |
dc.identifier.orcid | https://orcid.org/0000-0001-5691-0124 | - |
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